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Vol. 12, No. 17, pp. 2791-2802, September 1, 1998

RESEARCH PAPER
Amino acid-amino acid contacts at the cooperativity interface of the bacteriophage lambda  and P22 repressors

Frederick W. Whipple, Emmeline F. Hou, and Ann Hochschild1

Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115 USA

The bacteriophage lambda  repressor and its relatives bind cooperatively to adjacent as well as artificially separated operator sites. This cooperativity is mediated by a protein-protein interaction between the DNA-bound dimers. Here we use a genetic approach to identify two pairs of amino acids that interact at the dimer-dimer interface. One of these pairs is nonconserved in the aligned sequences of the lambda  and P22 repressors; we show that a lambda  repressor variant bearing the P22 residues at these two positions interacts specifically with the P22 repressor. The other pair consists of a conserved ion pair; we reverse the charges at these two positions and demonstrate that, whereas the individual substitutions abolish the interaction of the DNA-bound dimers, these changes in combination restore the interaction of both lambda cI and P22c2 dimers.

[Key Words: Charge reversal mutants; cooperativity; lambda repressor; P22 repressor; mutant-suppressor pairs; protein-protein interactions]

GENES & DEVELOPMENT 12:2791-2802 © 1998 by Cold Spring Harbor Laboratory Press  ISSN 0890-9369/98 $5.00
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